Specific receptors for retinol (alcohol form of vitamin A) but not retinoic acid (acid form of vitamin A) have been found in the cytosol if corneal epithelium derived from calf and cattle. The receptor migrates as a discrete peak of bound retinol in the 2S (approximately 20,000 M.W.) region in sucrose density gradients. As assessed by gel filtration the elution profile of the tissue is different from that observed with serum. After partial purification by gel filtration the tissue receptor complex was subjected to disc gel electrophoresis and was noted to migrate differently from retinol receptors present in serum. A limited number of higher affinity binding sites for retinol are present since incorporation of tritiated retinol into the epithelial receptor peak is markedly reduced by addition of excess non-radiolabelled vitamin A alcohol. The concentrated supernatant from pooled calf corneal stromas also exhibits a 2S receptor peak which is similar to that observed with corneal epithelium on sucrose density gradient centrifugation. Immunodiffusion studies performed with an antiserum which cross reacts with monkey serum retinol-binding protein failed to detect the presence of the serum protein in the cytosol of monkey corneal epithelium and the supernatant of pooled corneal stromas. Characterization to date in bovine and porcine tissues has demonstrated many similarities to the 2S tissue cytosol receptors previously demonstrated in retina and pigment epithelium.